Abstract
A peptide sequence with affinity to silica-containing materials was fused to a truncated form of Streptococcus strain G148 Protein G. The resulting recombinant Linker-Protein G (LPG) was produced in Escherichia coli and purified to apparent homogeneity. It displayed high affinity towards two natural clinoptilolite zeolites. The LPG also displayed high binding affinity towards commercial-grade synthetic zeolite, silica and silica-containing materials. A commercial sample of the truncated Protein G and a basic protein, both without the linker, did not bind to natural or synthetic zeolites or silica. We conclude that the zeolite-binding affinity is mediated by the linker peptide sequence. As a consequence, these data may imply that the binding affinity is directed to the SiO2 component rather than to the atomic orientation on the zeolite crystal surface as previously assumed.
| Language | English |
|---|---|
| Pages | 485-492 |
| Number of pages | 8 |
| Journal | New Biotechnology |
| Volume | 30 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 25 Jun 2013 |
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A linker peptide with high affinity towards silica-containing materials. / Sunna, Anwar; Chi, Fei; Bergquist, Peter L.
In: New Biotechnology, Vol. 30, No. 5, 25.06.2013, p. 485-492.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - A linker peptide with high affinity towards silica-containing materials
AU - Sunna, Anwar
AU - Chi, Fei
AU - Bergquist, Peter L.
PY - 2013/6/25
Y1 - 2013/6/25
N2 - A peptide sequence with affinity to silica-containing materials was fused to a truncated form of Streptococcus strain G148 Protein G. The resulting recombinant Linker-Protein G (LPG) was produced in Escherichia coli and purified to apparent homogeneity. It displayed high affinity towards two natural clinoptilolite zeolites. The LPG also displayed high binding affinity towards commercial-grade synthetic zeolite, silica and silica-containing materials. A commercial sample of the truncated Protein G and a basic protein, both without the linker, did not bind to natural or synthetic zeolites or silica. We conclude that the zeolite-binding affinity is mediated by the linker peptide sequence. As a consequence, these data may imply that the binding affinity is directed to the SiO2 component rather than to the atomic orientation on the zeolite crystal surface as previously assumed.
AB - A peptide sequence with affinity to silica-containing materials was fused to a truncated form of Streptococcus strain G148 Protein G. The resulting recombinant Linker-Protein G (LPG) was produced in Escherichia coli and purified to apparent homogeneity. It displayed high affinity towards two natural clinoptilolite zeolites. The LPG also displayed high binding affinity towards commercial-grade synthetic zeolite, silica and silica-containing materials. A commercial sample of the truncated Protein G and a basic protein, both without the linker, did not bind to natural or synthetic zeolites or silica. We conclude that the zeolite-binding affinity is mediated by the linker peptide sequence. As a consequence, these data may imply that the binding affinity is directed to the SiO2 component rather than to the atomic orientation on the zeolite crystal surface as previously assumed.
UR - http://www.scopus.com/inward/record.url?scp=84880144306&partnerID=8YFLogxK
U2 - 10.1016/j.nbt.2012.11.022
DO - 10.1016/j.nbt.2012.11.022
M3 - Article
VL - 30
SP - 485
EP - 492
JO - New Biotechnology
T2 - New Biotechnology
JF - New Biotechnology
SN - 1871-6784
IS - 5
ER -